構造解析ソフトウェアRELION (Sjors Scheres, MRC-LMB)を中心としたデータ解析講習会をオンライン開催いたします。

クライオ電子顕微鏡によるタンパク質の単粒子解析に興味をお持ちの方、実際にご自身では解析されたことがない初心者の方を対象にしています。
講習会では、RELIONのチュートリアルに沿って解説および座学を実施する予定です。開催者側でオンライン利用できる解析環境を用意いたします。参加者の方には実際に手を動かして、解析の流れを経験していただきます。

【開催日時】

1日目：2026年2月19日（木）10:00 〜 17:45 終了予定
※1日目18:00 〜 19:00 オンライン懇親会
2日目：2026年2月20日（金）10:00 〜 17:45 終了予定

【会場】

オンライン開催（Zoom）
講習会にアクセスするためのZoom URLは、参加登録時にお申込みいただきましたメールアドレスにお送りいたします。開催日が近づきましたら改めて個別にご案内をさせていただきます。

【言語】

日本語

【応募〆切 2026年1月26日（月）15:00】

申し込みはこちら

【募集対象と人数】

本講習会は、クライオ電子顕微鏡解析のご経験がないか、ほとんど無い方を対象としています。なお、学生の方は指導教員に了解を得ていただきますようお願いします。

定員：20名 （解析計算実行環境のリソースに限りがあるため、人数の制限をさせていただいています。予め、 ご了承ください。）

【参加条件】

今回の講習会は、クラウドコンピューター(AWS)上にRelionによる解析環境を開催者側で用意し、そこに参加者の皆様のパソコンからインターネットを通じてアクセスし、解析していただくことになります。従って、高性能のCPUやGPUを掲載したノートパソコンをご使用になる必要はございません。通常、ラボでデータ取りまとめ用などで使われているものでも、十分お使いいただけるものと考えています。Windows、Mac、どちらでも構いません。

民間企業の方のご出席につきましては、KEKのCryoEMコンソーシアム参加企業の方に限定させて頂いております。コンソーシアムへの入会は随時受付けておりますので、ご入会方法の詳細などについては下記の事務局連絡先までお気軽にお問い合わせください。

【参加費】

参加費：無料、その他の補助はありません。

【講師一覧】

川崎政人：KEK・物質構造科学研究所・構造生物学研究センター
守屋俊夫：KEK・物質構造科学研究所・構造生物学研究センター
中村　司：KEK・物質構造科学研究所・構造生物学研究センター
藤井裕己：KEK・物質構造科学研究所・構造生物学研究センター

【関連事業】

創薬等先端支援技術基盤プラットフォーム（BINDS）

【主催】

KEK・物質構造科学研究所・構造生物学研究センター
クライオ電顕ネットワーク

【プログラム】

プログラムの詳細は後日公開いたします。
前回のプログラムはこちら

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＊プログラムの変更があった場合は、随時更新します＊

2026年2月19日（木）

10:00-10:10　はじめに　（KEK）
-17:45 　

18:00-19:00　懇親会（オンライン）

　

2026年2月20日（金）

10:00-10:10　
14:40-15:10 写真撮影、休憩

17:20-17:25　終わりに（KEK）

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【 問い合わせ】

オーガナイザー
KEK・物質構造科学研究所・構造生物学研究センター
藤井裕己
E-mail: yufujii[at]post.kek.jp　

事務局
KEK・物質構造科学研究所・構造生物学研究センター
増田千穂 
電話：029-879-6176
E-mail: cmasuda[at]post.kek.jp

“From Plaques to Pores: In Situ Architecture and Isoform-Specific Gating of Human Gap Junction Channels”

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Date and Time

4:00 PM – 5:30 PM Thursday, January 22^nd, 2026

Location

Hybrid（CryoEM building and Zoom）

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Speaker

Juha Huiskonen

Professor of Structural Biology, University of Helsinki
Director of the Institute of Biotechnology (HiLIFE – Helsinki Institute of Life Science)
Member of the Molecular and Integrative Biosciences Research Programme
Head of the Laboratory of Structural Biology at the Institute of Biotechnology

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Abstract

Gap junction channels formed by connexins underpin electrical and biochemical coupling across tissues, yet the structural principles that govern their assembly and gating remain only partially defined. I will present two complementary structural studies that bridge native-membrane organization with atomic-level mechanisms of channel function. Our in situ cryo-ET structure of human Cx43 gap junction plaques at 14 Å reveals how the extensive C-terminal domain mediates lateral channel interactions critical for plaque formation. Supported by molecular simulations, we identify lipid and cholesterol densities between channels, resolving long-standing questions about the molecular determinants of gap junction lattice organization. In parallel, cryo-EM structures of human Cx45 in apo and Ca²⁺-bound forms at near-atomic resolution describe a compact and uniquely shaped pore, distinct N-terminal conformations, and C-terminal–intracellular loop interactions that define an isoform-specific gating mechanism. Ca²⁺ binding stabilizes a new conformation of E41 without inducing global motion, highlighting a subtle regulatory mechanism consistent with a semi-closed state.
Together, these findings contribute to an integrated view of connexin biology, revealing how structural diversity across isoforms and spatial organization within plaques contribute to tissue-specific modes of intercellular communication.

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“Targeting Asparagine Synthetase: Structural and Cellular Mechanisms of the Small-Molecule Inhibitor ASX-173”

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Date and Time

4:00 PM – 5:30 PM Wednesday, December 17^th, 2025

Location

Hybrid（CryoEM building and Zoom）

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Speaker

Yuichiro H. Takagi, Ph.D.

Associate Professor
Scientific advisor for cryo-EM 
Department of Biochemistry and Molecular Biology
Indiana University School of Medicine

Takagi Lab

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Abstract

Targeting asparagine metabolism is a promising strategy for treating asparaginase-resistant acute lymphoblastic leukemia (ALL), sarcoma, and potentially other solid tumors. Here, we characterize the molecular mechanism by which a cell-penetrable small molecule, ASX-173, inhibits human asparagine synthetase (ASNS), the enzyme that catalyzes intracellular asparagine biosynthesis. ASX-173 reduces cellular asparagine levels, induces the integrated stress response (ISR), and reduces cell growth in HEK-293A cells. A cryo-EM structure reveals that ASX-173 engages a unique, hydrophobic pocket formed by AMP, Mg2+, and pyrophosphate in the C-terminal synthetase domain of ASNS, thereby enabling multivalent, high-affinity binding. Based on in vitro kinetic and thermal shift assays, we find that ASX-173 binds to the ASNS/Mg2+/ATP complex and is therefore a rare example of an uncompetitive enzyme inhibitor with potential therapeutic use. These findings provide a structural and mechanistic basis for targeting ASNS with small molecules, which have application in treating cancer and other human diseases.

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“Using phase diagrams with microseeding to prepare crystal samples for advanced data collection techniques”

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Date and Time

2:00 PM – 3:00 PM Tuesday, December 9^th, 2025

Location

Hybrid（CryoEM building and Zoom）

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Speakers: Patrick D. Shaw Stewart

Douglas Instruments Ltd（UK）
University of Southampton（UK）

Abstract

Serial data collection and microED techniques typically require “slurries” of tiny, well-ordered crystals [1]. Neutron diffraction requires very large single crystals. Creating samples for these techniques is often a complex process that requires multiple rounds of optimization. To guide them in this task, protein crystallizers often keep a notional phase diagram in mind, which has four zones: an undersaturated zone where protein always remains in solution, a metastable zone where crystals will grow when seeds are added, a crystal nucleation zone where crystals appear spontaneously, and a protein precipitation zone. However, the shape of real-life phase diagrams can vary, making the interpretation of experimental results difficult. It is therefore very helpful to determine the phase diagrams of individual target proteins experimentally. Douglas Instruments, in collaboration with the University of Southampton, has introduced a rapid and straightforward method for generating custom phase diagrams using just 15 – 60 µL of protein [Fig. 1]. The most straightforward approach utilizes the microbatch-under-oil method to prevent concentrating the sample drop (as would occur in a vapor diffusion setup). By carrying out the same procedure with and without a seedstock, the metastable zone can be identified [2]. Moreover, advanced methods often require relatively large sample volumes, and microbatch can easily be scaled up to 50 µL or larger “batches” using robotics. A new variation of the method eliminates the need for oil by using a sitting drop setup, where solutions are dispensed to the reservoirs that exactly balance the concentrations of the drops. We present case studies where phase diagrams were utilized to enhance control and crystal quality for both routine and advanced data collection.

Figure 1.  The rapid determination of a protein’s phase diagram using　a microbatch-under-oil format.  Blue circles indicate the conditions that were tested.  Images of the wells are shown in conditions of interest. All points on the accessible phase diagram can be reached by mixing the three ingredients shown: protein stock (red circle), precipitant or cocktail stock (green circle) and a diluent, normally water (cyan circle).  To find the border of the metastable zone (dotted line) the experiment was repeated with the addition of a seed-stock (results not shown).

[1] Stubbs, J., Hornsey, T., Hanrahan, L.B. Esteban, R. Bolton, M.
Maly, S. Basu, J. Orlans, D. de Sanctis, J. Shim, Shaw Stewart, P. D.,
A.M. Orville, I. Tews and West, J. (2024). IUCrJ  11.

[2] D’Arcy, A., Villard, F., Marsh, M.  (2007). Acta Cryst. D63(4):550-4.

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“Structural Studies of Viral Macromolecular Complexes by Cryo-Electron Microscopy ”

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Date and Time

4:00 PM – 5:30 PM Friday, October 3^th, 2025

Location

Onsite（CryoEM building）

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Speakers: Yoko Fujita-Fujiharu

Postdoc
Max Planck Institute of Biochemistry
German,

Abstract

Understanding the architecture of viral macromolecular complexes is essential for elucidating the mechanisms of viral assembly and replication. While traditional structural biology often focuses on purified proteins in isolation, cryo-electron microscopy (cryo-EM) has the potential to analyze three-dimensional structures in more biologically relevant contexts.

In this talk, I will present some results from a study integrating multi-scale structural information of Ebola virus-like particles (VLPs). By combining in situ single-particle analysis and cryo-electron tomography, we resolved the structures of the viral matrix protein VP40 and the glycoprotein GP within intact VLPs. This multi-scale cryo-EM approach provides structural insights ranging from angstrom-level atomic detail to nanometer-scale organization, offering a more comprehensive understanding of viral assembly and function.

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